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Information on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase and Organism(s) Bacillus subtilis and UniProt Accession P30949

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.3 Transferring amino groups
                5.4.3.8 glutamate-1-semialdehyde 2,1-aminomutase
IUBMB Comments
Requires pyridoxal phosphate.
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This record set is specific for:
Bacillus subtilis
UNIPROT: P30949
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
gsa-at, glutamate 1-semialdehyde aminotransferase, gsa aminotransferase, glutamate-1-semialdehyde aminotransferase, glutamate-1-semialdehyde aminomutase, glutamate-1-semialdehyde 2,1-aminomutase, glutamate-1-semialdehyde-2,1-aminomutase, atgsa1, pa4088, glutamate-1-semialdehyde amino-transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamate-1-semialdehyde aminomutase
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Glutamate-1-semialdehyde aminotransferase
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Aminotransferase, glutamate semialdehyde
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Glutamate 1-semialdehyde aminotransferase
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-
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Glutamate-1-semialdehyde aminotransferase
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-
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GSA
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GSA aminotransferase
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-
-
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GSA-AT
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
(S)-4-amino-5-oxopentanoate 4,5-aminomutase
Requires pyridoxal phosphate.
CAS REGISTRY NUMBER
COMMENTARY hide
68518-07-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-glutamate 1-semialdehyde
5-aminolevulinate
show the reaction diagram
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-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on
pyridoxamine 5'-phosphate
dependent on
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with pyridoxamine 5'-phosphate, hanging drop vapor diffusion method, using 0.1 M Bicine pH 8.5, 30% (w/v) PEG 3350, at 23°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-chelating resin column chromatography and Superdex 200 gel filtration
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lv, X.; Fan, J.; Ge, H.; Gao, Y.; Zhang, X.; Teng, M.; Niu, L.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the glutamate-1-semialdehyde aminotransferase from Bacillus subtilis
Acta Crystallogr. Sect. F
62
483-485
2006
Bacillus subtilis
Manually annotated by BRENDA team
Ge, H.; Lv, X.; Fan, J.; Gao, Y.; Teng, M.; Niu, L.
Crystal structure of glutamate-1-semialdehyde aminotransferase from Bacillus subtilis with bound pyridoxamine-5-phosphate
Biochem. Biophys. Res. Commun.
402
356-360
2010
Bacillus subtilis (P30949), Bacillus subtilis
Manually annotated by BRENDA team